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1eo4

ECORV BOUND TO MN2+ AND COGNATE DNA CONTAINING A 3'S SUBSTITION AT THE CLEAVAGE SITE

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TYPE II RESTRICTION ENZYME ECORV

Escherichia coli

UniProt P04390

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Homooligomer Protein 2 DNA 2 ;DNA (5'-D(*CP*AP*AP*GP*AP*(TSP)P*AP*TP*CP*TP*T)-3') ; × 2 MANGANESE (II) ION × 5 ACETIC ACID × 2 water × 4 Consistent with all polymers

Other States of the Same Protein in the Database

Monomer

None

Homodimer
1az3 1az4 1rve

3 assemblies

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1az0 1b94 1b95 1b96 1b97 1bgb 1bss 1bsu 1bua 1eo3 1eo4 1eon

31 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name T2E5_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain A； PDBConstruct 2–245； UniProt 1–244 Author chain B； PDBConstruct 2–245； UniProt 1–244

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1eo4
Deposition date deposition_date2000-03-21
Structure title titleECORV BOUND TO MN2+ AND COGNATE DNA CONTAINING A 3'S SUBSTITION AT THE CLEAVAGE SITE
Keywords keywordsProtein-DNA complex, restriction endonuclease, DNA analog, hydrolase-DNA COMPLEX; hydrolase/DNA
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1eo4__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1eo4__assembly_1__model_1 | I(q)

10-2 10-1 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1eo4__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）23.83 Å
Rg (electron density)23.32 Å
Total Rg24.00 Å
Atom count4212
Residues492
Excluded volume73572 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1eo4__assembly_1__model_1 tetrameric （4） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1eo4a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.52 — Restriction endonuclease-like
Superfamily Superfamily superfamilyc.52.1 — Restriction endonuclease-like
Family Family familyc.52.1.2 — Restriction endonuclease EcoRV
Domain ID domain_idd1eo4b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.52 — Restriction endonuclease-like
Superfamily Superfamily superfamilyc.52.1 — Restriction endonuclease-like
Family Family familyc.52.1.2 — Restriction endonuclease EcoRV

CATH v4.4 (2 domains)

Domain ID domain_id1eo4A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — DNA mismatch repair MutH/Restriction endonuclease, type II
Domain ID domain_id1eo4B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — DNA mismatch repair MutH/Restriction endonuclease, type II
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7. Citations (1)